Related Experiment Video
Updated: Feb 1, 2026

Screening Assays to Characterize Novel Endothelial Regulators Involved in the Inflammatory Response
Published on: September 15, 2017
The STRIPAK complex components FAM40A and FAM40B regulate endothelial cell contractility via ROCKs
Narendra Suryavanshi1, Joanna Furmston1, Anne J Ridley2,3
1Randall Centre for Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, UK.
The FAM40 proteins are crucial for endothelial cell function and vascular integrity. They interact with CCM3, impacting barrier permeability and angiogenesis, suggesting a role in cerebral cavernous malformations (CCM).
Area of Science:
- Cell Biology
- Vascular Biology
- Protein Complexes
Background:
- Endothelial cells form a regulated barrier between blood and tissues.
- Cerebral cavernous malformations (CCM) involve dilated, leaky blood vessels, often linked to CCM3 mutations.
- CCM3 is part of the STRIPAK protein complex, including FAM40A and FAM40B.
Purpose of the Study:
- To investigate the interaction and function of FAM40A and FAM40B with CCM3.
- To determine the role of FAM40 proteins in endothelial cell physiology and vascular integrity.
Main Methods:
- RNA interference (RNAi) to deplete CCM3, FAM40A, or FAM40B in endothelial cells.
- Assessment of stress fibers and in vitro angiogenesis (loop formation).
- Measurement of endothelial permeability and inhibition of Rho-regulated ROCK kinases.
Main Results:
- FAM40A and FAM40B interact with CCM3.
- Depletion of CCM3, FAM40A, or FAM40B increased stress fibers and reduced angiogenesis.
- FAM40B depletion increased endothelial permeability, effects reversible by ROCK kinase inhibition.
Conclusions:
- FAM40 proteins are essential for endothelial cell function.
- FAM40 proteins likely function within the CCM3-STRIPAK complex.
- Dysregulation of FAM40 proteins may contribute to vascular pathologies like CCM.
More Related Videos
13:34Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip
Published on: September 29, 2012
14:33Simplified, High-throughput Analysis of Single-cell Contractility using Micropatterned Elastomers
Published on: April 8, 2022
Related Concept Videos
The Contractile Ring
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
pH Regulation in Cells
Cytosolic pH
Under physiological conditions, the cytosolic pH is slightly more acidic than the extracellular pH. However, cells must prevent further acidification of their cytosol to...
Regulated Protein Degradation
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Positive Regulator Molecules